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Investigation of wool protein heterogeneity using two-dimensional electrophoresis with immobilised pH gradients

✍ Scribed by Ben R. Herbert; Anna L. P. Chapman; Douglas A. Rankin

Publisher: John Wiley and Sons
Year: 1996
Tongue: English
Weight: 488 KB
Volume: 17
Category: Article
ISSN: 0173-0835
DOI: 10.1002/elps.1150170141

No coin nor oath required. For personal study only.

✦ Synopsis

Investigation of wool protein heterogeneity using two-dimensional electrophoresis with immobilised pH

Wool Research Organisation gradients of New Zealand, Christchurch, New Zealand

The heterogeneity of intermediate filament proteins (IFP) from wool has been investigated using two-dimensional polyacrylamide gel electrophoresis with immobilised pH gradients in the first dimension. The charge heterogeneity has been confirmed with some of the IFP separated as a string of spots with similar molecular weight, but markedly different in isoelectric point (pl). The molecular weight and p l distribution of the string of IFP changed after treatment with alkaline phosphatase, indicating that some of the heterogeneity is caused by phosphorylation.

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